Effects of adrenergic agonists on the extrahepatic expression of vitellogenin Ao1 in heart and brain of the Chinese rare minnow (Gobiocypris rarus)

Teleost vitellogenins (VTGs) are large multidomain apolipoproteins and traditionally considered as the estrogen responsive precursors of the major egg yolk proteins. We identified five clones encoding VTGs, about 16% of the random EST clones from our constructed cDNA library from Chinese rare minnow liver tissue treated with 17 beta-estradiol (E2). Full-length vtgAo1 has been obtained based on the sequence information of four partial cDNA inserts by RACE. The inducibility of the vtgAo1 expression in liver by E2 was confirmed by RT-PCR. The presence of vtgAo1 transcripts have been observed primarily in liver. However. a significant level of the vtgAo1 was found in an unexpected location, heart, particularly in atrial cells by RT-PCR and whole mount in situ hybridization analyses. The vtgAo1 mRNA expression in heart and liver tissue could be suppressed by both alpha-adrenergic agonist, phenylephrine (PE) and beta-adrenergic agonist, isoproterenol (ISO). The expression of VTG in the heart observed in the present studies suggested it may provide protection from surplus intracellular lipids in fish cardiomyocytes as triglyceride transport proteins do in mammals. The results also indicated that the production of teleost vtg in vivo can be regulated by riot only estrogenic agents, but adrenergic signals as well. (c) 2008 Elsevier B.V. All rights reserved.

Distribution of microcystins in various organs (heart, liver, intestine, gonad, brain, kidney and lung) of Wistar rat via intravenous injection

The distribution of microcystins (MCs) in various tissues of Wistar rats was studied under laboratory conditions. Rats were injected intravenously (i.v.) with extracted MCs at a dose of 80 mu g MC-LRequivalent/kg body weight. MCs concentrations in various tissues were detected at 1, 2. 4, 6, 12 and 24 h post-injection using liquid chromatography-mass spectrometry (LC-MS). The highest concentration of MCs was found in kidney (0.034-0.295 mu g/g dry weight), followed by lung (0.007-0.067 mu g/g dry weight), stomach (0.010-0.058 mu g/g dry weight) and liver (0.003-0.052 mu g/g dry weight). The maximum MCs content in the whole body of rat, 2.9% of the injected dose, was observed at 2 h post-injection. MCs concentration was higher in kidney than in liver during the experiment, and two peaks of MCs concentration (at 2 and 24 h, respectively) were observed in kidney, indicating that MCs can be excreted directly via kidney of rat. Though heart, intestine, spleen, brain, gonad and stomach contained less than 0.2% of injected MCs during the whole experiment stage, the presence of MCs in these tissues represents potential damage to them. (c) 2008 Elsevier Ltd. All Fights reserved.

In vivo studies on the toxic effects of microcystins on mitochondrial electron transport chain and ion regulation in liver and heart of rabbit

This study examined the toxic effects of microcystins on mitochondria of liver and heart of rabbit in vivo. Rabbits were injected i.p. with extracted microcystins (mainly MC-RR and -LR) at two doses, 12.5 and 50 MCLReq. mu g/kg bw, and the changes in mitochondria of liver and heart were studied at 1, 3,12, 24 and 48 h after injection. MCs induced damage of mitochondrial morphology and lipid peroxidation in both liver and heart. MCs influenced respiratory activity through inhibiting NADH dehydrogenase and enhancing succinate dehydrogenase (SDH). MCs altered Na+-K+-ATPase and Ca2+-Mg2+-ATPase activities of mitochondria and consequently disrupted ionic homeostasis, which might be partly responsible for the loss of mitochondrial membrane potential (MMP). MCs were highly toxic to mitochondria with more serious damage in liver than in heart. Damage of mitochondria showed reduction at 48 h in the low dose group, suggesting that the low dose of MCs might have stimulated a compensatory response in the rabbits. (C) 2008 Elsevier Inc. All rights reserved.

Effects of annealing on properties of spin-valve pinned with FeMn alloy

The magnetic properties of spin-valve pinned by FeMn layer were investigated after it was annealed at different temperatures. Its property was dependent on the vacuum annealing temperature. The pinning field could be increased through annealing at a temporature lower than 200degreesC;the pinning field would reduce and other properties be deteriorated as the annealing temperature was higher than 200degreesC; the pinning effect lost and giantmagnetic resistance disappeared at 300degreesC. Based on the results of AES analysis it was concluded that the diffusion in spin-valve multilayer was along grain boundary.

Magnetic property and interlayer segregation in spin valve metal multilayers

The experimental results show that the exchange coupling field of NiFe/FeMn for Ta/ NiFe/FeMn/Ta multilayers is higher than that for the spin valve multilayers Ta/NiFe/Cu/NiFe/FeMn/ Ta. In order to find out the reason, the composition and chemical states at the surfaces of Ta(12nm)/ NiFe(7nm), Ta(12nm)/NiFe(7nm)/Cu(4nm) and Ta(12nm)/NiFe(7nm)/Cu(3nm)/NiFe(5nm) were studied using the X-ray photoelectron spectroscopy (XPS). The results show that no elements from lower layers float out or segregate to the surface for the first and second samples. However, Cu atoms segregate to the surface of Ta(12nm)/NiFe(7nm)/Cu(3nm)/NiFe(5nm) multilayers, i.e. Cu atoms segregate to the NiFe/FeMn interface for Ta/NiFe/Cu/NiFe/FeMn/Ta multilayers. We believe that the presence of Cu atoms at the interface of NiFe/FeMn is one of the important factors causing the exchange coupling field of Ta/NiFe/FeMn/Ta multilayers to be higher than that of Ta/NiFe/Cu/NiFe/ FeMn/Ta multilayers.

Interlayer segregation of Cu atoms in Ta/NiFe/Cu/NiFe/FeMn/Ta spin-valve multilayers and its influence on magnetic properties

Experimental results show that the exchange coupling field (H-ex) of NiFe/FeMn for Ta/NiFe/FeMn/Ta multilayers is higher than that for spin-valve multilayers Ta/NiFe/Cu/NiFe/FeMn/Ta. In order to find out the reason, the composition and chemical states at the surface of Ta(12 nm)/NiFe(7 nm), Ta(12 nm)/NiFe(7 nm)/Cu(4 nm), and Ta(12 nm)/NiFe(7 nm)/Cu(3 nm)/NiFe(5 nm) were studied using x-ray photoelectron spectroscopy. The results show that no elements from lower layers float out or segregate to the surface in the first and second samples. However, Cu atoms segregate to the surface of Ta(12 nm)/NiFe(7 nm)/Cu(3 nm)/NiFe(5 nm) multilayers, i.e., Cu atoms segregate to the NiFe/FeMn interface for Ta/NiFe/Cu/NiFe/FeMn/Ta multilayers. We believe that the presence of Cu atoms at the interface of NiFe/FeMn is one of the important factors which causes the exchange coupling field (H-ex) of Ta/NiFe/Cu/NiFe/FeMn/Ta to be weaker than that of Ta/NiFe/FeMn/Ta. (C) 2002 American Institute of Physics.

Species；valve size；and pretreatment effects on delta O-18 and delta C-13 values of ostracod valves from Lake Qinghai；Qinghai-Tibet Plateau

IEECAS SKLLQG

Direct electron transfer reaction of horse heart hemoglobin at the indium oxide electrode

A direct, quasi-reversible electrochemical reaction of horse heart hemoglobin without further purification was obtained for the first time at the indium oxide electrode when oxygen was removed from the solution and hemoglobin molecules. It was found that removing oxygen from the solution and hemoglobin molecules is an important factor for obtaining the quasi-reversible electrochemical reaction of hemoglobin.

Electrochemical identification of intermediate forms of urea denaturation of horse heart cytochrome c

The electrochemical identification of the urea denaturation of horse heart cytochrome c in bulk solution at the 4,4'-dithiodipyridine-modified gold electrode is reported. The results are similar to the three-step transitions of equilibrium studies (Myer et al., Biochemistry, 19 (1980) 199) of urea denaturation of cytochrome c in bulk solution. This method permits a clear resolution of which of the three steps of urea denaturation is electrochemically related. In addition, by analysing the effects of urea on the structural forms of cytochrome c and on the solution properties, as well as the cyclic voltammetric responses of the protein, the individual forms of the urea denaturation of cytochrome c can be understood. The results reflect the superposition of protein denaturation on the electrode surface and in solution.

Effects of hypoxia on contents of essential elements in pika and rat heart

The effects of hypoxia on the levels of essential macroelements and trace elements (K, Na, Ca, Mg, Cu, Zn, Fe, and Mn) in the heart muscles of Wistar rats and plateau pikas (Ochotona curzoniae) were studied by atomic absorption spectrometry. Unlike the rat, the plateau pika is tolerant to hypoxia. The levels of K, Na, and the trace element Mn were not significantly changed in rat or pika hearts after exposure to hypoxia for 1, 10, or 25 d at simulated altitudes of 5000 and 7000 m. Other minerals (Ca, Mg, Cu, Zn, and Fe) were significantly affected by hypoxia and the levels followed different time-courses under different hypoxic regimes in these two animals. There were marked differences between the rat and pika in myocardial accumulation of essential elements such as Ca, which was increased to high levels in the rat but not affected in the pika. The results suggest that hypoxia affects animal physiological mechanisms by regulating the levels of essential elements.